• Journal of Dairy Science and Biotechnology
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• v.27 no.1
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• pp.19-28
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• 2009

Lactoferrin was first identified 60 years ago as a "red protein" in bovine milk. Lactoferrin, one of the transferrin family proteins, is an iron-binding glycoprotein found in milk and various mucosal secretions; it is also released from activated neutrophils. Human lactoferrin has a molecular weight of 82.4 kDa and is composed of 702 or 692 amino acid residues. Bovine lactoferrin has a molecular weight of 83.1 kDa and is composed of 689 amino acid residues. Both lactoferrin and transferrin have the ability to bind two $Fe^{3+}$ ions, together with two ${CO_3}^{2-}$ ions with extremely high affinity; these proteins also have the ability to release this iron at low pH levels. The polypeptide chain in lactoferrin is folded into two globular lobes, representing the N-terminal and C-terminal halves. Both lobes have similar folding and 40% sequence identity. This protein is capable of multiple functions as described in various review papers, including antimicrobial, antiviral, antiinflammatory, anticancer, antioxidant, and cell growth-promoting activities. Lactoferrin also exhibits immunomodulating effects and plays an active role in the regulation of myelopoiesis and the inhibition of bacterial translocation.

• Food Science of Animal Resources
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• v.28 no.4
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• pp.408-414
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• 2008

Low-fat sausages (LFS) containing various levels (0, 0.3, and 0.6%) of activated lactoferrin (ALF) which was prepared by dialysis to chelate irons of native lactoferrin, were manufactured and measured the physicochemical and textural properties, and shelf-life effect during refrigerated storage ($8^{\circ}C$). LFSs contained 72-16% moisture, 1-2% fat, 12-14% protein and a pH range of 6.04-6.08. No differences in physico-chemical and textural properties were observed with the increased ALF (p>0.05). Microbial growth of Listeria monocytogenes (LM), which inoculated at the levels of $10^4$ CFU/g, was increased with increased storage time. ALF at the amount of 0.6% slightly inhibited the microbial growth on the LFS (p<0.05), as compared to those of LFSs without ALF, however it had lower antimicrobial activity than those of 3.3% sodium lactate. These results indicated that the addition of ALF at the level of 0.6% affected the antibacterial activity of LFSs, resulting in the suppression of microbial growth in LFSs without quality defects.

• Journal of Periodontal and Implant Science
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• v.23 no.1
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• pp.48-55
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• 1993

Macrophage inflammatory $protein-1{\alpha}(MIP-1{\alpha})$ from activated T cell or macrophage, which is small inducible cytokine of unkown biological function, has been shown to display inflammation chemokinetic activities, as well as myelosuppressive effect on more immature progenitor cells. In this paper we show the $MIP-1{\alpha}$ mRNA expression and the presence of $MIP-1{\alpha}$ binding sites from murine macrophage cell line RAW 264.7, and primary cells of mouse bone marrow and spleen. $MIP-1{\alpha}$ mRNA was induced from LPS-stimulated RAW 264.7, but not inhibited by cyclosporin A treatment, and also was expressed from mouse splenocyted and bone marrow cell which were not increased by ferritin or lactoferrin treatment. The results of receptor binding assay showed that radiolabeled RAW 264.7 cell with kd value of 0.91 nM, and binding sites per cell of 378. bone marrow cell and splenocyte also appeared to have $MIP-1{\alpha}$ binding sites 33 and 11 per cell, respectiviely.